Chicken polymeric immunoglobulin of IgM from serum, and IgA from bile and intestinal contents were purified and characterized for their subunit compositions.
It was found that two IgM with different molecular weight of 860, 000 and 680, 000 daltons were present in chicken serum and that these two IgM were considered to be pentameric and tetrameric IgM, respectively. Both IgA from bile and intestinal contents showed the same molecular weight of 560, 000 daltons and were estimated to have trimeric structure.
Presence of J-chain was confirmed only in polymeric immunoglobulins of IgM and IgA but not in IgG by alkaline-urea-polyacrylamide gel electrophoresis. One J-chain was found per mole of polymeric immunoglobulin by subunit analyses of chicken biliary IgA.
Neither additional antigenic determinants nor a special protein moiety due to a putative chicken secretory components (SC) could be verified in IgA from various secretions by both immunological and sodium dodecyl sulfate polyacrylamide gel electrophoretic analyses.
Two light-chains with different molecular weight were found by sodium dodecyl sulfate acrylamide gel electrophoresis of chicken IgG, IgA and IgM. These two light-chains were assumed to be corresponded to two isotypes of chicken light-chains of IgY (G), reported recently.15)
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